› 2vew

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B IN COMPLEX WITH AN ISOTHIAZOLIDINONE-CONTAINING INHIBITOR

Released:
DOI: 10.2210/pdb2vew/pdb
PDB entry 2vew coloured by chain, front view.
PDB entry 2vew coloured by chain, side view.
PDB entry 2vew coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Isothiazolidinone inhibitors of PTP1B containing imidazoles and imidazolines.
Douty B, Wayland B, Ala PJ, Bower MJ, Pruitt J, Bostrom L, Wei M, Klabe R, Gonneville L, Wynn R, Burn TC, Liu PC, Combs AP, Yue EW
Bioorg Med Chem Lett 18 66-71 (2008)
PMID: 18037290

Function and Biology Details

Reaction catalysed: 
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase non-receptor type 1 Chain: A
Molecule details ›
Chain: A
Length: 321 amino acids
Theoretical weight: 37.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P18031 (Residues: 1-321; Coverage: 74%)
Gene names: PTP1B, PTPN1
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:
Ligand IZ3 1 x IZ3
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 66.8Å b: 72.72Å c: 88.13Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.201 0.239
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Protein tyrosine phosphatase 1B inhibitors: a molecular level legitimate approach for the management of diabetes mellitus.
Thareja et al. (2012)
4 more

3 mentions without citation

New Frontiers in Druggability.
Kozakov et al. (2015)
2 more